Noncompetitive allosteric inhibitors of the inflammatory chemokine receptors CXCR1 and CXCR2: Prevention of reperfusion injury

Riccardo Bertini, Marcello Allegretti, Cinzia Bizzarri, Alessio Moriconi, Massimo Locati, Giuseppe Zampella, Maria N. Cervellera, Vito Di Cioccio, Maria C. Cesta, Emanuela Galliera, Fernando O. Martinez, Rosa Di Bitondo, Giulia Troiani, Vilma Sabbatini, Gaetano D'Anniballe, Roberto Anacardio, Juan C. Cutrin, Barbara Cavalieri, Fabrizio Mainiero, Raffaele StrippoliPia Villa, Maria Di Girolamo, Franck Martin, Marco Gentile, Angela Santoni, Daniela Corda, Giuseppe Poli, Alberto Mantovani, Pietro Ghezzi, Francesco Colotta

Research output: Contribution to journalArticlepeer-review

Abstract

The chemokine CXC ligand 8 (CXCL8)/IL-8 and related agonists recruit and activate polymorphonuclear cells by binding the CXC chemokine receptor 1 (CXCR1) and CXCR2. Here we characterize the unique mode of action of a small-molecule inhibitor (Repertaxin) of CXCR1 and CXCR2. Structural and biochemical data are consistent with a noncompetitive allosteric mode of interaction between CXCR1 and Repertaxin, which, by locking CXCR1 in an inactive conformation, prevents signaling. Repertaxin is an effective inhibitor of polymorphonuclear cell recruitment in vivo and protects organs against reperfusion injury. Targeting the Repertaxin interaction site of CXCR1 represents a general strategy to modulate the activity of chemoattractant receptors.

Original languageEnglish
Pages (from-to)11791-11796
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume101
Issue number32
DOIs
Publication statusPublished - Aug 10 2004

ASJC Scopus subject areas

  • Genetics
  • General

Fingerprint

Dive into the research topics of 'Noncompetitive allosteric inhibitors of the inflammatory chemokine receptors CXCR1 and CXCR2: Prevention of reperfusion injury'. Together they form a unique fingerprint.

Cite this